Valine–tRNA ligase
class of enzymes
In enzymology, a valine–tRNA ligase (EC 6.1.1.9) is an enzyme that catalyzes the chemical reaction
ATP + L-valine + tRNAVal
⇌
{\displaystyle \rightleftharpoons }
AMP + diphosphate + L-valyl-tRNAVal
The 3 substrates of this enzyme are ATP, L-valine, and tRNAVal, whereas its 3 products are AMP, diphosphate, and L-valyl-tRNAVal. In humans, this enzyme is encoded by the genes VARS1 and VARS2.
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-valine:tRNAVal ligase (AMP-forming). Other names in common use include valyl-tRNA synthetase, valyl-transfer ribonucleate synthetase, valyl-transfer RNA synthetase, valyl-transfer ribonucleic acid synthetase, valine transfer ribonucleate ligase, and valine translase. This enzyme participates in valine, leucine and isoleucine biosynthesis, and aminoacyl-tRNA biosynthesis.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1GAX, PDB: 1IVS, PDB: 1IYW, PDB: 1WK9, and PDB: 1WKA.
See also
VARS
References
Berg P, Bergmann FH, Ofengand EJ, Dieckmann M (1961). "The enzymic synthesis of amino acyl derivatives of ribonucleic acid I. The mechanism of leucyl-, valyl-, isoleucyl- and methionyl ribonucleic acid formation". J. Biol.
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